BMRB Entry 34059

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34059
MolProbity Validation Chart

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Title:
Spatial structure of antimicrobial peptide arenicin-1 mutant V8R
Deposition date:
2016-11-02
Original release date:
2017-07-21
Authors:
Myshkin, M.; Shenkarev, Z.; Panteleev, P.; Ovchinnikova, T.
Citation:

Citation: Panteleev, P.; Myshkin, M.; Shenkarev, Z.; Ovchinnikova, T.. "Dimerization of the antimicrobial peptide arenicin plays a key role in the cytotoxicity but not in the antibacterial activity."  Biochem. Biophys. Res. Commun. 482, 1320-1326 (2017).
PubMed: 27940358

Assembly members:

Assembly members:
entity_1, polymer, 21 residues, 2824.409 Da.

Natural source:

Natural source:   Common Name: Lugworm   Taxonomy ID: 6344   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Arenicola marina

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: RWCVYAYRRVRGVLVRYRRC W

Data sets:
Data typeCount
13C chemical shifts79
15N chemical shifts29
1H chemical shifts168

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 21 residues - 2824.409 Da.

1   ARGTRPCYSVALTYRALATYRARGARGVAL
2   ARGGLYVALLEUVALARGTYRARGARGCYS
3   TRP

Samples:

sample_1: arenicin-1 V8R, [U-99% 15N], 1.8 mM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker AvanceI 700 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks